proteins polysaccharides and lipids Flashcards

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1
Q

what are examples of secondary structures?

A
  • a helix
  • b pleated sheet
  • triple helix
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2
Q

what is the a-helix?

A

Rod-like, right-handed
Found in strong, extensible proteins
Stabilised by hydrogen bonds
CO of each amino acid is H-bonded to NH of amino acid four residues ahead in sequence
3.6 residues/helix turn

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3
Q

what are examples of where alpha helixes are found?

A

haemoglobin, myoglobin, keratins, fibrins, myosin

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4
Q

what is a b-pleated sheet?

A

Zigzag chains
Place several chains side by side, CO and NH groups align, H-bonding occurs → sheet-like structure
Parallel: chains run in same direction
Anti-parallel: chains run in opposite directions
Found in proteins where flexibility needed

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5
Q

where is an example of where b- pleated sheets are found?

A

silk fibroin

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6
Q

what is a triple helix?

A

Collagen only
Major component of connective tissue (skin, bone, tendon)
Very strong, water-insoluble fibres
Three chains wound round each other (rope) → tropocollagen
~ 1000 amino acids per chain
No H bonds in each individual chain
Each chain has repeating structure:
X-Pro-Gly or X-Hyp-Gly
Three strands held together by H bonds between Hyp and hydroxylysine residues
Small Gly residue sits inside helix; bulky R groups either side of Gly project outwards
Intra- and inter-molecularly cross-linked by covalent bonds between Lys and His

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6
Q

what is a triple helix?

A

Collagen only
Major component of connective tissue (skin, bone, tendon)
Very strong, water-insoluble fibres
Three chains wound round each other (rope) → tropocollagen
~ 1000 amino acids per chain
No H bonds in each individual chain
Each chain has repeating structure:
X-Pro-Gly or X-Hyp-Gly
Three strands held together by H bonds between Hyp and hydroxylysine residues
Small Gly residue sits inside helix; bulky R groups either side of Gly project outwards
Intra- and inter-molecularly cross-linked by covalent bonds between Lys and His

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7
Q

what are fibrous proteins?

A

Insoluble
Metabolically unreactive
Principally structural proteins

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8
Q

what are examples of fibrous proteins?

A

collagen
keratin (skin, hair, nails, fur, wool)
fibrin (bloot clots)
elastin (elastic fibres of connective tissue eg. arterial walls)
myosin (muscle)

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9
Q

what are examples of fibrous proteins?

A

collagen
keratin (skin, hair, nails, fur, wool)
fibrin (bloot clots)
elastin (elastic fibres of connective tissue eg. arterial walls)
myosin (muscle)

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10
Q

what are globular proteins?

A

Spherical
Backbone folds on itself
Water-soluble, compact structures
Usually have tertiary and quaternary structures eg. myoglobin and actin (3º), haemoglobin (4º)

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11
Q

what is an example of a globular protein?

A

myoglobin, haemoglobin

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12
Q

what is myoglobin?

A
  • Oxygen storage in muscle
  • Globular, associated with 3º structures
  • Single chain (153 aa)
  • Contains eight helical regions (75% of all aa)
  • No β-pleated sheet regions
  • Helical segments joined by regions of random coiling where chain makes a major directional change
  • Interior contains entirely non-polar residues except for two polar His residues (attachment and function of haem group)
  • Prosthetic haem group: in hydrophobic pocket, held in position by hydrophobic interactions between haem porphyrin ring and non-polar side chains of aa in surrounding helical segments
  • Absence of haem group → apoprotein, not as tightly folded
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13
Q

what is haemoglobin?

A
  • Oxygen transport
  • Associated with 4º structures
  • Two pairs of polypeptide chains (2α, 2β) folded in a shape similar to myoglobin
  • Spheroidal molecule
  • Four haem groups lie on surface of molecule in individual pockets, far apart
  • α-chain = 141 aa; β-chain = 146 aa
  • Each α subunit is in contact with both β chains
  • Few interactions occur between the two α or the two β chains
  • α1β1 and α2β2 half-molecules irregular in shape → central open channel when fitted together
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14
Q

what are the types of membrane proteins?

A

peripheral- membrane surface
integral- within lipid bilayer
channel proteins
carrier proteins

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15
Q

what is the function of a channel protein?

A
  • forms a channel through the membrane
  • facilitates movements of small molecules across the membrane (simple diffusion)
16
Q

what is the function of carrier proteins?

A

bind to transported molecules (facilitated diffusion)

17
Q

what is an example of a messenger protein?

A

hormones

18
Q

what is the function of messenger proteins?

A

allows cells to communicate with each other

19
Q

describe the modes of action of messenger proteins

A
  • Influence rate of synthesis of enzymes and other proteins
  • Affect rate of enzymatic catalysis
  • Alter permeability of cell membranes
20
Q

describe the stages of hormones acting as messenger proteins

A

Each hormone has its own corresponding membrane-bound receptor

Hormone binds receptor → message relayed to inside of cell → cascade of events → cellular action

21
Q

what are examples of hormone messenger proteins and what are their functions?

A

Insulin: sugar uptake by cells from bloodstream
Glucagon: sugar release by cells into bloodstream
Human growth hormone

Hormones can be protein / polypeptide,
amino acid derivatives or steroid

22
Q

what are enzymes?

A

Biological catalysts
Globular proteins
Increase reaction rates by up to 1020
Highly specific (reaction, substrate)

23
Q

what is the difference in roles of myosin and actin during muscle contraction?

A
  • myosin is fibrous
  • actin is globular
24
Q

what are antibodies and cytokines involved in?

A

immune protection

25
Q

what are monosaccharides?

A

building blocks of complex carbohydrates (sugars)

26
Q

what are polymers made up of?

A

monomars

27
Q

what are the functions of polysaccharides?

A
  • storage eg glycogen and starch
  • structure eg cellulose, chondroitin sulphate, peptidoglycan
27
Q

what are the functions of polysaccharides?

A
  • storage eg glycogen and starch
  • structure eg cellulose, chondroitin sulphate, peptidoglycan
28
Q

what are the two groups within monosaccharides?

A

Aldoses: contain aldehyde group (CHO) eg glucose
Ketoses: contain ketone group (CO) eg fructose

29
Q

what is a disaccharide?

A

two monosaccharides joined together eg maltose

Dehydration / hydrolysis reactions of monosaccharide units form / catabolise complex carbohydrates

30
Q

describe the polysaccharide starch

A
  • amylose: unbranched (5-600 glucose units), α-1,4 linked
  • amylopectin: branched glucose units (up to 50,000), 30 α-1,4 linked units until branch point (α-1,6 link)
  • food reserve
31
Q

describe the polysaccharide glycogen

A
  • same structure as starch but more highly branched
  • food reserve
32
Q

describe the polysaccharide cellulose

A
  • unbranched β-1,4 linked glucose units
  • cannot be digested by animals enzymes (some ruminants possess β-glycosidases which digest cellulose)
  • structural role
33
Q

what are the monomers of lipids?

A

fatty acids

34
Q

what are the main types of lipids?

A
  • triglycerides- storage eg tristearin and glycerol
  • diglycerides- membrane structure eg phosphatidylcholine
  • sterols- membrane structure eg cholesterol
34
Q

what are the main types of lipids?

A
  • triglycerides- storage eg tristearin and glycerol
  • diglycerides- membrane structure eg phosphatidylcholine
  • sterols- membrane structure eg cholesterol
35
Q

what is a major component of biological membranes?

A

diacylglycerides

36
Q

what are the function of sterols?

A

Some have essential biological activity
Others are important constituents of biological membranes